ID A0A100IR87_ASPNG Unreviewed; 590 AA.
AC A0A100IR87;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Isoamyl alcohol oxidase {ECO:0000313|EMBL:GAQ45852.1};
GN ORFNames=ABL_08513 {ECO:0000313|EMBL:GAQ45852.1};
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061 {ECO:0000313|EMBL:GAQ45852.1, ECO:0000313|Proteomes:UP000068243};
RN [1] {ECO:0000313|Proteomes:UP000068243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An76 {ECO:0000313|Proteomes:UP000068243};
RX PubMed=26893421; DOI=10.1128/genomeA.01700-15;
RA Gong W., Cheng Z., Zhang H., Liu L., Gao P., Wang L.;
RT "Draft genome sequence of Aspergillus niger strain An76.";
RL Genome Announc. 4:E0170015-E0170015(2016).
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00005466}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAQ45852.1}.
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DR EMBL; BCMY01000018; GAQ45852.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A100IR87; -.
DR PaxDb; 5061-CADANGAP00007529; -.
DR VEuPathDB; FungiDB:An09g01320; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1130252; -.
DR VEuPathDB; FungiDB:ATCC64974_6930; -.
DR VEuPathDB; FungiDB:M747DRAFT_332621; -.
DR OMA; RCVGNEG; -.
DR Proteomes; UP000068243; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR Gene3D; 3.30.465.10; -; 2.
DR InterPro; IPR012951; BBE.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR PANTHER; PTHR13878; GULONOLACTONE OXIDASE; 1.
DR PANTHER; PTHR13878:SF91; L-GULONOLACTONE OXIDASE 3; 1.
DR Pfam; PF08031; BBE; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..590
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007087666"
FT DOMAIN 109..295
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 590 AA; 63984 MW; A245A2D0BD3BFEAC CRC64;
MFLSSILLLA GAQSVFAKCK CAPTDECWPS IDTWSALNSS VDGKLARNEP IAKPCYQGPG
YSSELCQRIS SNWTSNEYLA EFPIGYSYPL VESCPPVNAT LAGYPQCDLG NYPVYSVKAT
TAADVAAGIK FARDHNVRLV VKNTGHDISQ RSQGYGSLSI WIKSIQDGLH YHDRYVPGNG
SCPSNWTGSA ITVGGGYVWQ DVYDFAATHG VIAVGGADPT VGVLGGFMQG GGHGPVSHFF
GLGADQVLEY RVVLASGQLV TANACQYADL FTALRGGGGG TYGVVLSATI KAHPTRPVLG
HNLDIVALNG NDDAVLNATG NIMSKLPALS DAGYSGTAIL SAIAGPLVYT HPFLNLLENN
STEALDSAKD AMNRLILDDL LPQNGTSYLA ISTFTTYPTF HAYYSSTHHT TPGSNRPIMA
SRLFDKQTLE SPKINLTSLL ETVTAQTVPN STLWATLFNI VAGGKVLESV PHTSVNPAWR
RSHLLFQQID VWPDNAGDEE IQQYRSDLTR IKLKAMKDMA PGMGTYLNEA DPYDPDWRQD
WFGDNYDWLA SVKKKYDPEN VFWCWRCVGN EGWQEVTGGA WFGPLCETRK
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